3QGK

3.0 A Model of Iron Containing Urease UreA2B2 from Helicobacter mustelae (refined w/ no ordered solvent)

Summary for 3QGK

• Entry DOI: 10.2210/pdb3qgk/pdb
• Related: 3QGA
• Descriptor: Fusion of urease beta and gamma subunits, Urease subunit beta 2, FE (III) ION (3 entities in total)
• Functional Keywords: iron metalloenzyme, alpha-beta barrel, urease, hydrolase
• Biological source: Helicobacter mustelae (Campylobacter mustelae); More
• Cellular location: Cytoplasm (By similarity): D3UJ80
• Total number of polymer chains: 12
• Total formula weight: 523521.65

Authors

Tronrud, D.E.,Robbins, A.,Karplus, P.A. (deposition date: 2011-01-24, release date: 2011-08-10, Last modification date: 2023-12-06)

Primary citation

Carter, E.L.,Tronrud, D.E.,Taber, S.R.,Karplus, P.A.,Hausinger, R.P.
Iron-containing urease in a pathogenic bacterium.
Proc.Natl.Acad.Sci.USA, 108:13095-13099, 2011

PubMed Abstract: Helicobacter mustelae, a gastric pathogen of ferrets, synthesizes a distinct iron-dependent urease in addition to its archetypical nickel-containing enzyme. The iron-urease is oxygen-labile, with the inactive protein exhibiting a methemerythrin-like electronic spectrum. Significantly, incubation of the oxidized protein with dithionite under anaerobic conditions leads to restoration of activity and bleaching of the spectrum. Structural analysis of the oxidized species reveals a dinuclear iron metallocenter bridged by a lysine carbamate, closely resembling the traditional nickel-urease active site. Although the iron-urease is less active than the nickel-enzyme, its activity allows H. mustelae to survive the carnivore's low-nickel gastric environment.

PubMed: 21788478
DOI: 10.1073/pnas.1106915108

Experimental method

X-RAY DIFFRACTION (3 Å)